WhiB2/Rv3260c, a cell division-associated protein of Mycobacterium tuberculosis H37Rv, has properties of a chaperone.

Konar, Monica and Alam, Md Suhail and Arora, Chandni and Agrawal, Pushpa (2012) WhiB2/Rv3260c, a cell division-associated protein of Mycobacterium tuberculosis H37Rv, has properties of a chaperone. The FEBS journal, 279 (15). pp. 2781-92. ISSN 1742-4658

PDF pushpa2012.pdf - Published Version Restricted to Registered users only Download (1702Kb) | Request a copy

Abstract

whiB-like genes have been found in all actinomycetes sequenced so far. The amino-acid sequences of WhiB proteins of Mycobacterium tuberculosis H37Rv are highly conserved and participate in several cellular functions. Unlike other WhiB proteins of M. tuberculosis that have properties of protein disulfide reductases, WhiB2 showed properties like a chaperone as it suppressed the aggregation of several model substrates (e.g. citrate synthase, rhodanese and luciferase). Suppression of aggregation of the model substrates did not require ATP. Four cysteine residues of WhiB2 form two intramolecular disulfide bonds; however, chaperone function was unaffected by the redox state of the cysteines. WhiB2 also restored the activity of chemically denatured citrate synthase and did not require either ATP or a co-chaperone for refolding. The results indicate that WhiB2, which has been shown to be associated with cell division in mycobacteria and streptomyces, has evolved independently of other WhiBs, although it retains basic properties of this group of proteins. This is the first report to show that a WhiB protein has chaperone-like function; therefore, this report will have major implications in attempts to understand the role of WhiB proteins in mycobacteria, particularly in cell division.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Wiley.
Uncontrolled Keywords:	chaperone; intramolecular disulfide bonds; Mycobacterium tuberculosis; WhiB2
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	28 Jan 2013 11:56
Last Modified:	28 Jan 2013 11:56
URI:	http://crdd.osdd.net/open/id/eprint/1241

Actions (login required)

View Item